8pk3

CryoEM reconstruction of hemagglutinin HK68 of Influenza A virus bound to an Affimer reagent

Method: ELECTRON MICROSCOPY Dmax: 154.8 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Hemagglutinin HA1 chain

Influenza A virus

UniProt Q91MA7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 9 其他Polymer 6 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 27–344 Chain B; UniProt 27–344 Chain C; UniProt 27–344 Not recorded Hemagglutinin HA2 chain × 3 (P03437) Affimer molecule (A31) × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

46 other PDB entries and 90 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEMA_I68A4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–322; UniProt 27–344 Author chain B; PDBConstruct 5–322; UniProt 27–344 Author chain C; PDBConstruct 5–322; UniProt 27–344

Hemagglutinin HA2 chain

Influenza A virus

UniProt P03437

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 9 其他Polymer 6 PDB declaration: nonameric(9) Consistent with protein copy count Chain D; UniProt 346–520 Chain E; UniProt 346–520 Chain F; UniProt 346–520 Not recorded Hemagglutinin HA1 chain × 3 (Q91MA7) Affimer molecule (A31) × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

42 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HEMA_I68A0
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–175; UniProt 346–520 Author chain E; PDBConstruct 1–175; UniProt 346–520 Author chain F; PDBConstruct 1–175; UniProt 346–520

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8pk3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pk3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8pk3
Deposition date deposition_date2023-06-24
Structure title titleCryoEM reconstruction of hemagglutinin HK68 of Influenza A virus bound to an Affimer reagent
Keywords keywordsComplex, Inhibitor, CryoEM, Antiviral, ANTIVIRAL PROTEIN; ANTIVIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier44.91
Radius of gyration Rg (electron density) rg_electron44.82
Forward intensity I(0) i0636361000.00
Molecular weight molecular_weight202870.0 kDa
Excluded volume excluded_volume251960 ų
Envelope volume envelope_volume343900 ų
Hydration-shell volume shell_volume66208 ų
Envelope diameter envelope_diameter167.5
Shell Rg shell_rg46.73
Envelope Rg envelope_rg45.09
Shape Rg shape_rg44.81
Total Rg total_rg44.94
Total atoms total_atoms14277
Residues n_residues1752
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax154.8
Rg (real space) rg_real45.17
Rg uncertainty (real space) rg_real_error1.53
I(0) (real space) i0_real6.3640e+08
I(0) uncertainty (real space) i0_real_error1.1250e+07
Rg (reciprocal space) rg_reciprocal44.91
I(0) (reciprocal space) i0_reciprocal636200000.0000
Solution quality estimate total_estimate0.8372
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.6
Skewness Skewness skewness0.522
Kurtosis Kurtosis kurtosis-0.182
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha59660000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.931; Smooth: 0.623

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)